This invention relates to a method and composition for inhibiting the growth of cancerous cells and tumors.
The enzymes known generically as glycosyltransferases participate in the biosynthesis of complex carbohydrates. They are commonly found as membrane-bound enzymes within the interior of the cell. The function of adding sugars to proteins is not clear, although the nature of the terminal sugar appears to be important in the control of secretion and in the clearance of circulating glycoproteins and the biosynthesis of ABO blood group substances also requires sugar additions through the action of glycosyltransferases. Although some glycosyltransferases appear to be membrane-associated enzymes when prepared from tissue homogenates, these transferases have also been detected as soluble enzymes in various body fluids, including rat and human serum.
It has been reported in Biochemical and Biophysical Research Communications, Vol. 65, No. 2, pp. 545-551 and proceedings of the National Academy of Sciences, U.S.A., Vol. 73, No. 4, pp. 1319-1322 that there exists two isoenzymes of serum galactosyltransferase. The isoenzyme identified as GT-II was shown to be found predominantly in patients with neoplastic disease. There is a correlation of serum GT-II levels with the extent of malignancy which apparently is independent of the site of the neoplasm. The preoperative level of GT-II activity appears to correlate with the overall extent of the tumor. Thus, the level of serum GT-II increases in association with the progression of the disease. It is not known whether the galactosyltransferase (GT-II) is merely produced by the cancerous cells or is somehow involved in the mechanism of cancerous cell reproduction.